From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2qfs.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2qfs.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2qfs| PDB=2qfs | SCENE= }} | | {{STRUCTURE_2qfs| PDB=2qfs | SCENE= }} |
| | | | |
| - | '''E.coli EPSP synthase Pro101Ser liganded with S3P'''
| + | ===E.coli EPSP synthase Pro101Ser liganded with S3P=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Glyphosate, the world's most used herbicide, is a massive success because it enables efficient weed control with minimal animal and environmental toxicity. The molecular target of glyphosate is 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS), which catalyzes the sixth step of the shikimate pathway in plants and microorganisms. Glyphosate-tolerant variants of EPSPS constitute the basis of genetically engineered herbicide-tolerant crops. A single-site mutation of Pro(101) in EPSPS (numbering according to the enzyme from Escherichia coli) has been implicated in glyphosate-resistant weeds, but this residue is not directly involved in glyphosate binding, and the basis for this phenomenon has remained unclear in the absence of further kinetic and structural characterization. To probe the effects of mutations at this site, E. coli EPSPS enzymes were produced with glycine, alanine, serine, or leucine substituted for Pro(101). These mutant enzymes were analyzed by steady-state kinetics, and the crystal structures of the substrate binary and substrate.glyphosate ternary complexes of P101S and P101L EPSPS were determined to between 1.5- and 1.6-A resolution. It appears that residues smaller than leucine may be substituted for Pro(101) without decreasing catalytic efficiency. Any mutation at this site results in a structural change in the glyphosate-binding site, shifting Thr(97) and Gly(96) toward the inhibitor molecule. We conclude that the decreased inhibitory potency observed for glyphosate is a result of these mutation-induced long-range structural changes. The implications of our findings concerning the development and spread of glyphosate-resistant weeds are discussed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17855366}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17855366 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17855366}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 27: |
Line 31: |
| | [[Category: Inside-out alpha-beta barrel]] | | [[Category: Inside-out alpha-beta barrel]] |
| | [[Category: Transferase]] | | [[Category: Transferase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:52:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:44:16 2008'' |
Revision as of 17:44, 28 July 2008
Template:STRUCTURE 2qfs
E.coli EPSP synthase Pro101Ser liganded with S3P
Template:ABSTRACT PUBMED 17855366
About this Structure
2QFS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase., Healy-Fried ML, Funke T, Priestman MA, Han H, Schonbrunn E, J Biol Chem. 2007 Nov 9;282(45):32949-55. Epub 2007 Sep 12. PMID:17855366
Page seeded by OCA on Mon Jul 28 20:44:16 2008
